1n64: Difference between revisions

Revision as of 13:10, 28 July 2008

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File:1n64.png

Template:STRUCTURE 1n64

Crystal structure analysis of the immunodominant antigenic site on Hepatitis C virus protein bound to mAb 19D9D6Crystal structure analysis of the immunodominant antigenic site on Hepatitis C virus protein bound to mAb 19D9D6

Template:ABSTRACT PUBMED 12574359

About this StructureAbout this Structure

1N64 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a hydrophobic immunodominant antigenic site on hepatitis C virus core protein complexed to monoclonal antibody 19D9D6., Menez R, Bossus M, Muller BH, Sibai G, Dalbon P, Ducancel F, Jolivet-Reynaud C, Stura EA, J Immunol. 2003 Feb 15;170(4):1917-24. PMID:12574359

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OCA

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-'''Crystal structure analysis of the immunodominant antigenic site on Hepatitis C virus protein bound to mAb 19D9D6'''
+===Crystal structure analysis of the immunodominant antigenic site on Hepatitis C virus protein bound to mAb 19D9D6===
-==Overview==
+<!--
-The first crystal structure of a complex between a hepatitis C virus (HCV) core protein-derived peptide (residues 13-40) and the Ab fragment of a murine mAb (19D9D6) has been solved, allowing determination of the recognized epitope and elucidation of its conformation. This Ab, raised against the first 120 residues of the core protein, recognizes core particles and strongly competes with anticore human Abs, suggesting that it is highly representative of the human anti-HCV core response. Its epitope lies within the first 45 aa of the protein, the major antigenic segment of core recognized both by murine and human Abs. Surprisingly, the recognized epitope (29-37: QIVGGVYLL) has an unusual preponderance of hydrophobic residues, some of which are buried in a small hydrophobic core in the nuclear magnetic resonance structure of the peptide (2-45) in solution, suggesting that the Ab may induce a structural rearrangement upon recognition. The flexibility may reside entirely within the Ag, since the Fab'-peptide complex structure at 2.34 A shows that the Ab binding site is hardly perturbed by complexation. Given that the recognized residues are unlikely to be solvent exposed, we are left with the interesting possibility that Ab-core interactions may take place in a nonaqueous environment.
+The line below this paragraph, {{ABSTRACT_PUBMED_12574359}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12574359}}
 ==About this Structure==
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 [[Category: Stura, E.]]
 [[Category: Antibody peptide complex]]
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